1LKB

Porcine Pancreatic Elastase/Na-Complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.203 
  • R-Value Work: 0.169 

Starting Model: experimental
View more details

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Metal binding to porcine pancreatic elastase: calcium or not calcium.

Weiss, M.S.Panjikar, S.Nowak, E.Tucker, P.A.

(2002) Acta Crystallogr D Biol Crystallogr 58: 1407-1412

  • DOI: https://doi.org/10.1107/S0907444902010934
  • Primary Citation of Related Structures:  
    1LKA, 1LKB

  • PubMed Abstract: 

    Porcine pancreatic elastase has been crystallized at slightly acidic pH under two similar but slightly different conditions. Diffraction data were collected at a wavelength of 1.5 A to a maximum resolution of 1.7 A. Both difference electron-density maps and anomalous difference electron-density maps suggest that in crystals grown from a sodium sulfate solution PPE binds Na(+) in its metal-binding site. In contrast, PPE binds Ca(2+) in crystals grown from a solution containing sodium citrate and calcium chloride. This observation is in contradiction to most PPE structures reported in the PDB. In addition to the metal-binding site, up to three other binding sites, which appear to be anion-binding sites, could be identified based on the observed anomalous intensity differences.


  • Organizational Affiliation

    EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany. [email protected]


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Elastase 1240Sus scrofaMutation(s): 0 
EC: 3.4.21.36
UniProt
Find proteins for P00772 (Sus scrofa)
Explore P00772 
Go to UniProtKB:  P00772
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00772
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.203 
  • R-Value Work: 0.169 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 50.17α = 90
b = 58.06β = 90
c = 74.34γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
TRUNCATEdata reduction
REFMACrefinement
CCP4data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-08-28
    Type: Initial release
  • Version 1.1: 2008-04-28
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-08-16
    Changes: Data collection, Database references, Derived calculations, Refinement description
  • Version 1.4: 2024-10-16
    Changes: Structure summary